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Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis

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We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

Dans ce travail, nous décrivons la purification et la caractérisation d’une nouvelle bactériocine, nommée thuricine S, produite par Bacillus thuringiensis subsp. entomocidus HD198. Cette activité antibactérienne est sensible à la protéinase K, résistante à la température et stable à une large gamme de pH (3–10,5). La masse de la thuricine S purifiée par la chromatographie liquide à haute pression, déterminée par spectrométrie de masse ESI-TOF-MS, est de 3137,61 Da. Le séquençage par la méthode d’Edman et par NanoESI-MS/MS a permis de déterminer les 18 acides aminés N-terminaux. La séquence N-terminale (DWTXWSXL) de cette bactériocine est identique à celles de la bacthuricine F4 et de la thuricine 17, produites respectivement par B. thuringiensis BUPM4 et B. thuringiensis NEB17. La thuricine S pourrait donc être classée comme une nouvelle bactériocine de la sous-classe IId.

Document Type: Research Article

Publication date: 2007-02-01

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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